1. Volume 11, Issue 9, Pages 1293-1299 (September 2004)
Identification of Novel Small-Molecule Inhibitors of Severe Acute Respiratory Syndrome- Associated Coronavirus by Chemical Genetics 
Richard Y. Kao, Wayne H.W. Tsui, Terri S.W. Lee, Julian A. Tanner, Rory M. Watt, Jian-Dong Huang, Lihong Hu, Guanhua Chen, Zhiwei Chen, Linqi Zhang, Tian He, Kwok-Hung Chan, Herman Tse, Amanda P.C. To, Louisa W.Y. Ng, Bonnie C.W. Wong, Hoi-Wah Tsoi, Dan Yang, David D. Ho, Kwok-Yung Yuen 
Chemistry & Biology 
Volume 11, Issue 9, Pages (September 2004)
DOI: /j.chembiol

2. Figure 1
Isolation of Biologically Active Small-Molecule Inhibitors of SARS-CoV in a Phenotype-Based Screen
A schematic illustration of major processes involved in the phenotype-based screen is shown. Enlarged images of Vero cells from a typical 384-well tissue culture plate used in screening are also included to indicate the criteria for hit selection. Only those compounds that fully protected the Vero cells from SARS-CoV-induced CPE were selected as hits.
Chemistry & Biology  , DOI: ( /j.chembiol )

3. Figure 2 MP576 Targets SARS-CoV Mpro
(A) MP576 inhibited in vitro cleavage activity of SARS-CoV Mpro with an IC50 of 2.5 μM. Synthetic peptide H2N-TSAVLQSGFRKW-COOH was used as the substrate in the assay.
(B) MP576 inhibited SARS-CoV plaque formation with an EC50 of 7 μM.
(C) MP576 is predicted to occupy the active site of SARS-CoV Mpro (left) and hydrogen bonds with Cys145 N and His41 Nϵ2 (right). The active site of SARS-CoV Mpro is shown as a surface model (left) and the backbone trace (light blue) of SARS-CoV is shown, along with the side chains of residues crucial for substrate binding and catalysis (right). MP576 carbons are shown in green. Predicted hydrogen bonds are shown as dashed lines.
(D) MP576 (100 μM) did not inhibit human neutrophil elastase (HNE). Azocasein was used as the substrate in the assay.
(E) Chemical structure of MP576 (3-quinolinecarboxylic acid, 1,4,5,6,7,8-hexahydro-2-methyl-4-(2-nitrophenyl)-5-oxo-, 2-phenylethyl ester).
Chemistry & Biology  , DOI: ( /j.chembiol )

4. Figure 3 HE602 Targets SARS-CoV Hel
(A) HE602 inhibited polynucleotide-stimulated ATPase activity of SARS-CoV Hel.
(B) HE602 (200 μM) did not inhibit significantly the nonstimulated ATPase activity.
(C) Inhibition of SARS-CoV Hel helicase activity by HE602 observed by polyacrylamide electrophoresis of labeled duplex and single-stranded DNA. The positions of the 32P-labeled DNA partial duplex and released single strand are indicated to the left of the polyacrylamide gel (the star indicates the position of the 32P label).
(D) HE602 inhibited SARS-CoV plaque formation with an EC50 of 6 μM.
(E) Chemical structure of HE602 (3-Benzyloxy-N-(4-chloro-3-oxazolo[4,5-b]pyridine-2-yl-phenyl)benzamide).
Chemistry & Biology  , DOI: ( /j.chembiol )

5. Figure 4 VE607 Blocks S Protein-ACE2-Mediated SARS-CoV Entry
(A) VE607 blocked SARS-CoV S protein pseudotype HIV-1 virus infection of 293T cells expressing ACE2 with an EC50 of 3 μM.
(B) VE607 inhibited SARS-CoV plaque formation with an EC50 of 1.6 μM.
(C) VE607 (10 μM) became ineffective when excluded from the plaque reduction assay at stage crucial for viral entry (0–2 hr postinfection).
(D) VE607 (50 μM) did not inhibit poliovirus plaque formation.
(E) Chemical structure of VE607 (1-[3-(2-Hydroxyl-3-piperidin-1-yl-propoxy)-phenoxy]-3-piperidin-1-ylpropan-2-ol).
Chemistry & Biology  , DOI: ( /j.chembiol )